A kinetic analysis of the glycolytic rate and certain glycolytic enzymes in normal and leucemic leucocytes.

It is generally agreed that human leucocytes have high aerobic glycolytic rates (1) and previous studies (2, 3) have shown the rates in homogenates of isolated normal leucocytes to be significantly higher than in leucemic cells. The present studies seek to explain this metabolic difference in terms of possible differences between the enzymic mechanisms of glycolysis in normal and leucemic leucocytes. Throughout the huge literature on glycolysis, it is often stated that the glycolytic rate of a tissue is determined by a single, rate-limiting step in the sequential chain of reactions although its identity is unknown. Nor is it known whether the rate-limiting step is the same in all tissues or whether it remains the same in pathological variants showing altered glycolytic rates. Some evidence has implicated the cell adenosine triphosphate-adenosine diphosphate ratio (4) as the determinant of glycolytic rate, a ratio at least partially controlled by the balance between adenosinetriphosphatase and hexokinase, but the data are inconclusive. Presumably, that ratio would influence the activity of adenylic acidlinked enzymes, one of which might then become rate-limiting. Burton (5) and Hinshelwood (6) have emphasized the possible hazards of the “master reaction” concept by pointing out that in a sequence of irreversible first order reactions